GenomeNet

Database: UniProt/TrEMBL
Entry: D2A2T2_TRICA
LinkDB: D2A2T2_TRICA
Original site: D2A2T2_TRICA 
ID   D2A2T2_TRICA            Unreviewed;       153 AA.
AC   D2A2T2;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   25-OCT-2017, entry version 55.
DE   RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000256|RuleBase:RU000393};
DE            EC=1.15.1.1 {ECO:0000256|RuleBase:RU000393};
GN   Name=SOD {ECO:0000313|EMBL:AKH80544.1};
GN   ORFNames=TcasGA2_TC007011 {ECO:0000313|EMBL:EFA02790.1};
OS   Tribolium castaneum (Red flour beetle).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Coleoptera; Polyphaga;
OC   Cucujiformia; Tenebrionidae; Tenebrionidae incertae sedis; Tribolium.
OX   NCBI_TaxID=7070 {ECO:0000313|EMBL:EFA02790.1, ECO:0000313|Proteomes:UP000007266};
RN   [1] {ECO:0000313|EMBL:EFA02790.1, ECO:0000313|Proteomes:UP000007266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA02790.1,
RC   ECO:0000313|Proteomes:UP000007266};
RX   PubMed=18362917; DOI=10.1038/nature06784;
RG   Tribolium Genome Sequencing Consortium;
RA   Richards S., Gibbs R.A., Weinstock G.M., Brown S.J., Denell R.,
RA   Beeman R.W., Gibbs R., Beeman R.W., Brown S.J., Bucher G.,
RA   Friedrich M., Grimmelikhuijzen C.J., Klingler M., Lorenzen M.,
RA   Richards S., Roth S., Schroder R., Tautz D., Zdobnov E.M., Muzny D.,
RA   Gibbs R.A., Weinstock G.M., Attaway T., Bell S., Buhay C.J.,
RA   Chandrabose M.N., Chavez D., Clerk-Blankenburg K.P., Cree A., Dao M.,
RA   Davis C., Chacko J., Dinh H., Dugan-Rocha S., Fowler G., Garner T.T.,
RA   Garnes J., Gnirke A., Hawes A., Hernandez J., Hines S., Holder M.,
RA   Hume J., Jhangiani S.N., Joshi V., Khan Z.M., Jackson L., Kovar C.,
RA   Kowis A., Lee S., Lewis L.R., Margolis J., Morgan M., Nazareth L.V.,
RA   Nguyen N., Okwuonu G., Parker D., Richards S., Ruiz S.J.,
RA   Santibanez J., Savard J., Scherer S.E., Schneider B., Sodergren E.,
RA   Tautz D., Vattahil S., Villasana D., White C.S., Wright R., Park Y.,
RA   Beeman R.W., Lord J., Oppert B., Lorenzen M., Brown S., Wang L.,
RA   Savard J., Tautz D., Richards S., Weinstock G., Gibbs R.A., Liu Y.,
RA   Worley K., Weinstock G., Elsik C.G., Reese J.T., Elhaik E., Landan G.,
RA   Graur D., Arensburger P., Atkinson P., Beeman R.W., Beidler J.,
RA   Brown S.J., Demuth J.P., Drury D.W., Du Y.Z., Fujiwara H.,
RA   Lorenzen M., Maselli V., Osanai M., Park Y., Robertson H.M., Tu Z.,
RA   Wang J.J., Wang S., Richards S., Song H., Zhang L., Sodergren E.,
RA   Werner D., Stanke M., Morgenstern B., Solovyev V., Kosarev P.,
RA   Brown G., Chen H.C., Ermolaeva O., Hlavina W., Kapustin Y.,
RA   Kiryutin B., Kitts P., Maglott D., Pruitt K., Sapojnikov V.,
RA   Souvorov A., Mackey A.J., Waterhouse R.M., Wyder S., Zdobnov E.M.,
RA   Zdobnov E.M., Wyder S., Kriventseva E.V., Kadowaki T., Bork P.,
RA   Aranda M., Bao R., Beermann A., Berns N., Bolognesi R., Bonneton F.,
RA   Bopp D., Brown S.J., Bucher G., Butts T., Chaumot A., Denell R.E.,
RA   Ferrier D.E., Friedrich M., Gordon C.M., Jindra M., Klingler M.,
RA   Lan Q., Lattorff H.M., Laudet V., von Levetsow C., Liu Z., Lutz R.,
RA   Lynch J.A., da Fonseca R.N., Posnien N., Reuter R., Roth S.,
RA   Savard J., Schinko J.B., Schmitt C., Schoppmeier M., Schroder R.,
RA   Shippy T.D., Simonnet F., Marques-Souza H., Tautz D., Tomoyasu Y.,
RA   Trauner J., Van der Zee M., Vervoort M., Wittkopp N., Wimmer E.A.,
RA   Yang X., Jones A.K., Sattelle D.B., Ebert P.R., Nelson D., Scott J.G.,
RA   Beeman R.W., Muthukrishnan S., Kramer K.J., Arakane Y., Beeman R.W.,
RA   Zhu Q., Hogenkamp D., Dixit R., Oppert B., Jiang H., Zou Z.,
RA   Marshall J., Elpidina E., Vinokurov K., Oppert C., Zou Z., Evans J.,
RA   Lu Z., Zhao P., Sumathipala N., Altincicek B., Vilcinskas A.,
RA   Williams M., Hultmark D., Hetru C., Jiang H., Grimmelikhuijzen C.J.,
RA   Hauser F., Cazzamali G., Williamson M., Park Y., Li B., Tanaka Y.,
RA   Predel R., Neupert S., Schachtner J., Verleyen P., Raible F., Bork P.,
RA   Friedrich M., Walden K.K., Robertson H.M., Angeli S., Foret S.,
RA   Bucher G., Schuetz S., Maleszka R., Wimmer E.A., Beeman R.W.,
RA   Lorenzen M., Tomoyasu Y., Miller S.C., Grossmann D., Bucher G.;
RT   "The genome of the model beetle and pest Tribolium castaneum.";
RL   Nature 452:949-955(2008).
RN   [2] {ECO:0000313|EMBL:EFA02790.1, ECO:0000313|Proteomes:UP000007266}
RP   GENOME REANNOTATION.
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA02790.1,
RC   ECO:0000313|Proteomes:UP000007266};
RX   PubMed=19820115; DOI=10.1093/nar/gkp807;
RA   Kim H.S., Murphy T., Xia J., Caragea D., Park Y., Beeman R.W.,
RA   Lorenzen M.D., Butcher S., Manak J.R., Brown S.J.;
RT   "BeetleBase in 2010: revisions to provide comprehensive genomic
RT   information for Tribolium castaneum.";
RL   Nucleic Acids Res. 38:D437-D442(2010).
RN   [3] {ECO:0000313|EMBL:EFA02790.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA02790.1};
RA   Shelton J.M., Herndon N., Coleman C., Lu N., Brown S.J.;
RT   "Tools and pipelines for BioNano data: molecule assembly pipeline and
RT   FASTA super scaffolding tool.";
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:AKH80544.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ANU101 {ECO:0000313|EMBL:AKH80544.1};
RA   Kim Y.;
RT   "Chlorine dioxide against Tribolium castaneum.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC       {ECO:0000256|RuleBase:RU000393}.
CC   -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC       {ECO:0000256|RuleBase:RU000393}.
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000256|RuleBase:RU000393};
CC       Note=Binds 1 copper ion per subunit.
CC       {ECO:0000256|RuleBase:RU000393};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU000393};
CC       Note=Binds 1 zinc ion per subunit.
CC       {ECO:0000256|RuleBase:RU000393};
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC       {ECO:0000256|RuleBase:RU000393}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; KP342269; AKH80544.1; -; mRNA.
DR   EMBL; KQ971339; EFA02790.1; -; Genomic_DNA.
DR   RefSeq; XP_015835141.1; XM_015979655.1.
DR   RefSeq; XP_968284.1; XM_963191.3.
DR   SMR; D2A2T2; -.
DR   STRING; 7070.TC007011-PA; -.
DR   EnsemblMetazoa; TC007011_001; TC007011_001; TC007011.
DR   GeneID; 656682; -.
DR   KEGG; tca:656682; -.
DR   eggNOG; KOG0441; Eukaryota.
DR   eggNOG; COG2032; LUCA.
DR   InParanoid; D2A2T2; -.
DR   KO; K04565; -.
DR   OMA; IHTFGDN; -.
DR   Proteomes; UP000007266; Linkage group 4.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR   CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
DR   Gene3D; 2.60.40.200; -; 1.
DR   InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR   InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
DR   InterPro; IPR018152; SOD_Cu/Zn_BS.
DR   InterPro; IPR001424; SOD_Cu_Zn_dom.
DR   PANTHER; PTHR10003; PTHR10003; 1.
DR   Pfam; PF00080; Sod_Cu; 1.
DR   PRINTS; PR00068; CUZNDISMTASE.
DR   SUPFAM; SSF49329; SSF49329; 1.
DR   PROSITE; PS00087; SOD_CU_ZN_1; 1.
DR   PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome {ECO:0000313|Proteomes:UP000007266};
KW   Copper {ECO:0000256|RuleBase:RU000393};
KW   Metal-binding {ECO:0000256|RuleBase:RU000393};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000393,
KW   ECO:0000313|EMBL:AKH80544.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007266};
KW   Zinc {ECO:0000256|RuleBase:RU000393}.
FT   DOMAIN       10    148       Sod_Cu. {ECO:0000259|Pfam:PF00080}.
SQ   SEQUENCE   153 AA;  15690 MW;  FFB1302956D3486E CRC64;
     MPTKAVCVLN GEVKGTIFFT QENGKAPVQV TGEVSGLKKG LHGFHIHEFG DNTNGCISAG
     AHFNPHGKDH GGPTHDVRHV GDLGNIEAGG DGVAKVGITD KFISLEGEHS IIGRTLVVHA
     DPDDLGQGGH ELSKTTGNAG ARLACGVVGI TKA
//
DBGET integrated database retrieval system